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Blood, 1 February 2007, Vol. 109, No. 3, pp. 1193-1201. Prepublished online as a Blood First Edition Paper on September 26, 2006; DOI 10.1182/blood-2006-03-012021. This Article Full Text Full Text (PDF) Supplemental Table All Versions of this Article: blood-2006-03-012021v1 109/3/1193    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Abrams, S. T. Articles by Slupsky, J. R. Search for Related Content PubMed PubMed Citation Articles by Abrams, S. T. Articles by Slupsky, J. R. Related Collections Neoplasia Signal Transduction Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  NEOPLASIA B-cell receptor signaling in chronic lymphocytic leukemia cells is regulated by overexpressed active protein kinase CßII Simon T. Abrams1, Tasneem Lakum1, Ke Lin1, Gemma M. Jones1, Andrew T. Treweeke1, Mosavar Farahani1, Mair Hughes1, Mirko Zuzel1, and Joseph R. Slupsky1 1 Department of Haematology, University of Liverpool, Liverpool, United Kingdom Signals through the B-cell antigen receptor (BCR) are important for the survival of chronic lymphocytic leukemia (CLL) cells. Therefore, factors that influence these signals have important pathophysiological roles in this disease. One key mediator of BCR signaling is protein kinase C ß (PKCß), which regulates the activation of I-B kinases and the deactivation of Bruton tyrosine kinase within the signaling pathways initiated by BCR engagement. The present study demonstrates that overexpression of the PKCßII isoform is a feature of CLL cells and that activity of this enzyme strongly correlates with CLL cell response to BCR engagement. Thus, intracellular Ca2+ release and increases in cell survival after BCR cross-linking were significantly greater in CLL patients with low levels than in CLL patients with high levels of active PKCßII. Furthermore, BCR-induced Ca2+ fluxes could be restored in CLL patients with high levels of active PKCßII by pretreating the cells with the PKCß-specific inhibitor LY379196. Conversely, BCR-mediated intracellular Ca2+ release could be inhibited in CLL cells with low levels of active PKCßII by pretreatment with the PKC agonist bryostatin. Taken together, these results demonstrate that overexpressed active PKCßII plays a role in the regulation and outcome of BCR signals that can be important for the progression of CLL. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Protein kinase C inhibitor enzastaurin induces in vitro and in vivo antitumor activity in Waldenström macroglobulinemia Anne-Sophie Moreau, Xiaoying Jia, Hai T. Ngo, Xavier Leleu, Garrett O'Sullivan, Yazan Alsayed, Alexey Leontovich, Klaus Podar, Jeffrey Kutok, John Daley, Suzan Lazo-Kallanian, Evdoxia Hatjiharissi, Marc S. Raab, Lian Xu, Steven P. Treon, Teru Hideshima, Kenneth C. Anderson, and Irene M. Ghobrial Blood 2007 109: 4964-4972. [Abstract] [Full Text] [PDF] This article has been cited by other articles: A.-S. Moreau, X. Jia, H. T. Ngo, X. Leleu, G. O'Sullivan, Y. Alsayed, A. Leontovich, K. Podar, J. Kutok, J. Daley, et al. Protein kinase C inhibitor enzastaurin induces in vitro and in vivo antitumor activity in Waldenstrom macroglobulinemia Blood, June 1, 2007; 109(11): 4964 - 4972. [Abstract] [Full Text] [PDF]

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